The Gamma 1 Heavy-chain Disease FOR Protein is Present in Two Molecular Forms

Overview

Journal Folia Microbiol (Praha)

Publisher Springer

Specialty Microbiology

Date 1984 Jan 1

PMID 6430761

Citations 1

Authors

J Zikan

L Rozprimova

J Novotny

Affiliations

Soon will be listed here.

Abstract

Heavy chain disease proteins (FOR) were isolated from human plasma. These proteins were also detected immunochemically in the urine of the patient. The proteins were disulphide-linked Fc-like dimers with molar mass 64.2 kg/mol and sedimentation rate S020,W = 0.356 ps (3.56 S). Similar amounts of aspartic acid and pyroglutamic acid were found at the N-terminus. After cyanogen bromide cleavage of the FOR proteins, three peptides were isolated and their amino acid composition and partial amino acid sequence was determined. We suggest that two Fc-like proteins of similar sizes are present in the plasma: (1) the first with N-terminal aspartic acid corresponding to position 221 of gamma 1 EU chain and (2) the second with N-terminal pyroglutamic acid. The first protein and small amounts of related low-molar mass fragments found also in the plasma could be degradation products of the second protein. Evidence is given on structural differences between the FOR proteins and the corresponding portion of the gamma 1 EU chain.

Citing Articles

[Gamma 1 heavy chain disease with immune vasculitis and rheumatoid arthritis].

Stuhlinger W, Berek K, Lapin A, Jaschke E, Pastner D Klin Wochenschr. 1987; 65(8):359-68.

PMID: 3108571 DOI: 10.1007/BF01745573.

References

FRANKLIN E, Prelli F, Frangione B . Human heavy chain disease protein WIS: implications for the organization of immunoglobulin genes. Proc Natl Acad Sci U S A. 1979; 76(1):452-6. PMC: 382958. DOI: 10.1073/pnas.76.1.452. View

Blackburn S, LOWTHER A . The separation of N-2:4-dinitrophenly amino-acids on paper chromatograms. Biochem J. 1951; 48(1):126-8. PMC: 1275301. DOI: 10.1042/bj0480126. View

Ponstingl H, Hilschmann N . [The rule of antibody structure. The primary structure of a monoclonal IgG1 immunoglobulin (myeloma protein Nie). III. The chymotryptic peptides of the H-chain, alignment of the tryptic peptides and discussion of the complete structure]. Hoppe Seylers Z Physiol Chem. 1976; 357(11):1571-604. View

KABAT E . THE MOLECULAR WEIGHT OF ANTIBODIES. J Exp Med. 2009; 69(1):103-18. PMC: 2133729. DOI: 10.1084/jem.69.1.103. View

Sakano H, Rogers J, Huppi K, Brack C, Traunecker A, Maki R . Domains and the hinge region of an immunoglobulin heavy chain are encoded in separate DNA segments. Nature. 1979; 277(5698):627-33. DOI: 10.1038/277627a0. View

Frangione B . A technique for the detection of deleted immunoglobulin heavy chains. Biochemistry. 1973; 12(17):3355-9. DOI: 10.1021/bi00741a033. View

Wilkinson J, PRESS E, Porter R . The N-terminal sequence of the heavy chain of rabbit immunoglobulin IgG. Biochem J. 1966; 100(2):303-8. PMC: 1265136. DOI: 10.1042/bj1000303. View

Biewenga J, Frangione B, FRANKLIN E, van Loghem E . A gamma l heavy-chain disease protein *EST) lacking the entire VH and CHl domains. Scand J Immunol. 1980; 11(6):601-7. DOI: 10.1111/j.1365-3083.1980.tb00028.x. View

Edelman G, Cunningham B, Gall W, Gottlieb P, Rutishauser U, Waxdal M . The covalent structure of an entire gammaG immunoglobulin molecule. Proc Natl Acad Sci U S A. 1969; 63(1):78-85. PMC: 534037. DOI: 10.1073/pnas.63.1.78. View

10.

FRANKLIN E, Frangione B . The molecular defect in a protein (CRA) found in gamma-1 heavy chain disease, and its genetic implications. Proc Natl Acad Sci U S A. 1971; 68(1):187-91. PMC: 391192. DOI: 10.1073/pnas.68.1.187. View

11.

Bennett J . The amino-terminal sequence of the heavy chain of human immunoglobulin M. Biochemistry. 1968; 7(10):3340-4. DOI: 10.1021/bi00850a005. View

12.

Moore S, STEIN W . Photometric ninhydrin method for use in the chromatography of amino acids. J Biol Chem. 1948; 176(1):367-88. View

13.

Woods K, Wang K . Separation of dansyl-amino acids by polyamide layer chromatography. Biochim Biophys Acta. 1967; 133(2):369-70. DOI: 10.1016/0005-2795(67)90078-5. View

14.

FRANKLIN E, Lowenstein J, BIGELOW B, Meltzer M . HEAVY CHAIN DISEASE- A NEW DISORDER OF SERUM GAMMA-GLOBULINS : REPORT OF THE FIRST CASE. Am J Med. 1964; 37:332-50. DOI: 10.1016/0002-9343(64)90191-3. View

15.

Weber K, Osborn M . The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969; 244(16):4406-12. View

16.

TERRY W, Ein D . Structural studies of gamma heavy chain disease proteins. Ann N Y Acad Sci. 1971; 190:467-71. DOI: 10.1111/j.1749-6632.1971.tb13556.x. View

17.

YPHANTIS D . EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS. Biochemistry. 1964; 3:297-317. DOI: 10.1021/bi00891a003. View

18.

Turner M, Martensson L, Natvig J, Bennich H . Genetic (Gm) antigens associated with subfragments from the Fc fragment of human immunoglobulin G. Nature. 1969; 221(5186):1166-9. DOI: 10.1038/2211166a0. View

19.

Skvaril F, Rejnek J . [Our experience with a micromodification of immunoelectrophoresis]. Cesk Epidemiol Mikrobiol Imunol. 1958; 7(6):414-7. View

20.

Frangione B, FRANKLIN E, SMITHIES O . Unusual genes at the aminoterminus of human immunoglobulin variants. Nature. 1978; 273(5661):400-1. DOI: 10.1038/273400a0. View